ID RFIP3_MOUSE Reviewed; 1047 AA.
AC Q8CHD8; Q8JZT3;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Rab11 family-interacting protein 3 {ECO:0000250|UniProtKB:O75154};
DE Short=FIP3 {ECO:0000303|PubMed:18685082};
DE Short=FIP3-Rab11 {ECO:0000250|UniProtKB:O75154};
DE Short=Rab11-FIP3 {ECO:0000250|UniProtKB:O75154};
GN Name=Rab11fip3 {ECO:0000312|MGI:MGI:2444431}; Synonyms=Kiaa0665;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 188-1047 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH ASAP1.
RX PubMed=18685082; DOI=10.1091/mbc.e08-03-0290;
RA Inoue H., Ha V.L., Prekeris R., Randazzo P.A.;
RT "Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and
RT regulates pericentrosomal localization of transferrin receptor-positive
RT recycling endosome.";
RL Mol. Biol. Cell 19:4224-4237(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Downstream effector molecule for Rab11 GTPase which is
CC involved in endocytic trafficking, cytokinesis and intracellular
CC ciliogenesis by participating in membrane delivery (PubMed:18685082).
CC Recruited by Rab11 to endosomes where it links Rab11 to dynein motor
CC complex. The functional Rab11-RAB11FIP3-dynein complex regulates the
CC movement of peripheral sorting endosomes (SE) along microtubule tracks
CC toward the microtubule organizing center/centrosome, generating the
CC endocytic recycling compartment (ERC) during interphase of cell cycle.
CC Facilitates the interaction between dynein and dynactin and activates
CC dynein processivity (By similarity). Binding with ASAP1 is needed to
CC regulate the pericentrosomal localization of recycling endosomes
CC (PubMed:18685082). The Rab11-RAB11FIP3 complex is also implicated in
CC the transport during telophase of vesicles derived from recycling
CC endosomes to the cleavage furrow via centrosome-anchored microtubules,
CC where the vesicles function to deliver membrane during late cytokinesis
CC and abscission. The recruitment of Rab11-RAB11FIP3-containing endosomes
CC to the cleavage furrow and tethering to the midbody is co-mediated by
CC RAB11FIP3 interaction with ARF6-exocyst and RACGAP1-MKLP1 tethering
CC complexes. Also involved in the Rab11-Rabin8-Rab8 ciliogenesis cascade
CC by facilitating the orderly assembly of a ciliary targeting complex
CC containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which
CC directs preciliary vesicle trafficking to mother centriole and
CC ciliogenesis initiation. Also promotes the activity of Rab11 and ASAP1
CC in the ARF4-dependent Golgi-to-cilia transport of the sensory receptor
CC rhodopsin. Competes with WDR44 for binding to Rab11, which controls
CC intracellular ciliogenesis pathway. May play a role in breast cancer
CC cell motility by regulating actin cytoskeleton (By similarity).
CC {ECO:0000250|UniProtKB:O75154, ECO:0000269|PubMed:18685082}.
CC -!- SUBUNIT: Homodimer. Interacts with RAB11A; the interaction is direct
CC and is required for the recruitment to endosomes. Interacts with
CC RAB11B. Forms a ternary complex with RAB11A and dynein intermediate
CC chain DYNC1LI1; RAB11FIP3 links RAB11A to dynein and the interaction
CC regulates endocytic trafficking. Interacts with dynein intermediate
CC chain and dynactin (DCTN1); the interaction activates dynein
CC processivity. Interacts with ARF6 and EXOC7; the interaction serves for
CC recruitment and tethering of recycling endosomes-derived vesicles to
CC the cleavage furrow/midbody. Interacts with RACGAP1/MgcRacGAP; the
CC interaction occurs at late telophase and is required for recruitment
CC and tethering of recycling endosomes-derived vesicles to the cleavage
CC furrow/midbody. Forms a complex with RAB11A and Rabin8/RAB3IP, probably
CC a heterohexamer with two of each protein subunit, where RAB3IP and
CC RAB11FIP3 simultaneously bind to RAB11A; the complex promotes
CC preciliary trafficking (By similarity). Forms a complex containing
CC RAB11A, ASAP1, RAB3IP, RAP11FIP3 and ARF4; the complex promotes
CC preciliary trafficking; the complex binds to RHO in photoreceptor cells
CC and promotes RHO ciliary transport (PubMed:18685082). Interacts with
CC RAB11FIP4. Interacts with RAB25 (By similarity).
CC {ECO:0000250|UniProtKB:O75154, ECO:0000269|PubMed:18685082}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:O75154}; Peripheral membrane protein
CC {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250|UniProtKB:O75154}. Cleavage furrow
CC {ECO:0000250|UniProtKB:O75154}. Midbody {ECO:0000250|UniProtKB:O75154}.
CC Golgi apparatus membrane {ECO:0000250|UniProtKB:O75154}; Peripheral
CC membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:O75154}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CHD8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHD8-2; Sequence=VSP_038667;
CC Name=3;
CC IsoId=Q8CHD8-3; Sequence=VSP_038668;
CC -!- DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (RAB11A
CC or RAB11B). {ECO:0000250|UniProtKB:O75154}.
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DR EMBL; AC140047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023364; AAH23364.1; -; mRNA.
DR EMBL; BC037132; AAH37132.1; -; mRNA.
DR EMBL; AB093257; BAC41441.1; -; mRNA.
DR CCDS; CCDS50039.1; -. [Q8CHD8-2]
DR CCDS; CCDS50040.1; -. [Q8CHD8-1]
DR CCDS; CCDS50041.1; -. [Q8CHD8-3]
DR RefSeq; NP_001156340.1; NM_001162868.1. [Q8CHD8-1]
DR RefSeq; NP_001156341.1; NM_001162869.1. [Q8CHD8-3]
DR RefSeq; NP_694780.1; NM_153140.2. [Q8CHD8-2]
DR AlphaFoldDB; Q8CHD8; -.
DR SMR; Q8CHD8; -.
DR BioGRID; 229626; 2.
DR IntAct; Q8CHD8; 1.
DR MINT; Q8CHD8; -.
DR STRING; 10090.ENSMUSP00000113521; -.
DR iPTMnet; Q8CHD8; -.
DR PhosphoSitePlus; Q8CHD8; -.
DR SwissPalm; Q8CHD8; -.
DR MaxQB; Q8CHD8; -.
DR PaxDb; 10090-ENSMUSP00000113521; -.
DR ProteomicsDB; 255296; -. [Q8CHD8-1]
DR ProteomicsDB; 255297; -. [Q8CHD8-2]
DR ProteomicsDB; 255298; -. [Q8CHD8-3]
DR Antibodypedia; 22705; 108 antibodies from 25 providers.
DR DNASU; 215445; -.
DR Ensembl; ENSMUST00000118828.8; ENSMUSP00000113048.2; ENSMUSG00000037098.19. [Q8CHD8-2]
DR Ensembl; ENSMUST00000120691.9; ENSMUSP00000112875.2; ENSMUSG00000037098.19. [Q8CHD8-1]
DR Ensembl; ENSMUST00000122103.9; ENSMUSP00000113521.2; ENSMUSG00000037098.19. [Q8CHD8-3]
DR Ensembl; ENSMUST00000148021.3; ENSMUSP00000119626.3; ENSMUSG00000037098.19. [Q8CHD8-2]
DR GeneID; 215445; -.
DR KEGG; mmu:215445; -.
DR UCSC; uc008bdc.2; mouse. [Q8CHD8-2]
DR UCSC; uc008bdd.2; mouse. [Q8CHD8-3]
DR UCSC; uc008bde.2; mouse. [Q8CHD8-1]
DR AGR; MGI:2444431; -.
DR CTD; 9727; -.
DR MGI; MGI:2444431; Rab11fip3.
DR VEuPathDB; HostDB:ENSMUSG00000037098; -.
DR eggNOG; KOG0982; Eukaryota.
DR GeneTree; ENSGT00440000033742; -.
DR HOGENOM; CLU_018925_2_0_1; -.
DR InParanoid; Q8CHD8; -.
DR OrthoDB; 5312348at2759; -.
DR PhylomeDB; Q8CHD8; -.
DR TreeFam; TF327221; -.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 215445; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Rab11fip3; mouse.
DR PRO; PR:Q8CHD8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CHD8; Protein.
DR Bgee; ENSMUSG00000037098; Expressed in right kidney and 216 other cell types or tissues.
DR Genevisible; Q8CHD8; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0030666; C:endocytic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0098944; C:postsynaptic recycling endosome membrane; IDA:SynGO.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051959; F:dynein light intermediate chain binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0070164; P:negative regulation of adiponectin secretion; ISO:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:1902954; P:regulation of early endosome to recycling endosome transport; ISS:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; ISS:UniProtKB.
DR GO; GO:1904779; P:regulation of protein localization to centrosome; ISS:UniProtKB.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; ISS:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.20.5.2440; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR037245; FIP-RBD_C_sf.
DR InterPro; IPR019018; Rab-bd_FIP-RBD.
DR PANTHER; PTHR15726:SF6; RAB11 FAMILY-INTERACTING PROTEIN 3; 1.
DR PANTHER; PTHR15726; RAB11-FAMILY INTERACTING PROTEIN; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF09457; RBD-FIP; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF144270; Eferin C-derminal domain-like; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51511; FIP_RBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Endosome; Golgi apparatus; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transport.
FT CHAIN 1..1047
FT /note="Rab11 family-interacting protein 3"
FT /id="PRO_0000390970"
FT DOMAIN 496..531
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 528..563
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 985..1047
FT /note="FIP-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..879
FT /note="ARF-binding domain (ABD)"
FT /evidence="ECO:0000250"
FT REGION 882..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 750..985
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 511
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 513
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75154"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75154"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75154"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75154"
FT VAR_SEQ 1..603
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12465718"
FT /id="VSP_038667"
FT VAR_SEQ 712
FT /note="P -> PSSNPLASKLCDVLTDEAFEFYCSQCHKQINRLEDLSARLTDLEMN
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038668"
SQ SEQUENCE 1047 AA; 118535 MW; 4A78951AFB9696C4 CRC64;
MELCQPTSLS DHDQPASGPQ RGVMGLVGPD APRGWSEEPE EHAQLQRWPE GPNAPICWPE
EVEEPHAPSR WAKEPNAPRC SSQEPDESCH LAEELEESDS PRCWPQEPDT PCHLAKELEE
PDAPRCLPQE PDTPCYLAKE LEEPNIPRCW PQEPDVPCHL AKELEEPDAP RCWPQEPDAF
CHLLKEVEEP DALRCWLQGP DAPCHLAKEL EDLDSPRCWP QEPDESCHLA KELEEPDAPC
HLAKELEEPD APRCWPQEPD VPCLLAKKWE ESDAPCLLTE ELEEPDALHC WPQESEAPCL
LAKELEEPDA SHSCPQEADT GCLSAKEPEE PDVSHLWQGV PDAPCLLVKE PEEADALHCC
WPEESEEPDA LNPPCFWANE PDEPDPSRCW SEEPQVLCLW PEEQNTKRCW QEEPDAPCFW
PEDREEPIVS CLQFKEPEKP KVRSSWPEEL EDCCPTRGLP LEPLLADGEL LQACPGPPSD
PGPALSLPSE PGTAQEEGAR LRAVFDALDR DGDGFVRIED FIQFATVYGA EQVKDLTQYL
DPSGLGVISF EDFYQGIVAI RNGDPDGQLY SVEPVQDEET PACADEFDDF VTYEANEVTD
SAYMGSESTY SECETFTDED TSTLVHPELQ PEGDVDSAGG SGVPSECLDT MEEPDHGALL
LLPGRSRPHS QAVVMVIGSE EHFEDYGEGN EAELSPETLC DGDGEDPAFL TPSPAKRLSS
RKVARYLHQS GTLTMEALED PPPEPVECPE EDIADKVIFL ERRVSELEKD SAAAGEQHGR
LRQENLQLVH RANALEEQLK EQEFRAQEKV LEETRKQKEL LCKMEREKSI EIENLQARLQ
QLDEENSELR SCTPCLKANI ERLEEEKQKM LDEIEELTQR LSEEQENKRK MGDRLSHERH
QFQRDKEATQ ELIEDLRKQL EHLQLLRLEV EQRRGRSSSL GLQEYNSRAR ESELEQEVRR
LKQDNRNLKE QNDELNGQII TLSIQGAKSL FSTSFSESLA AEISSVSRDE LMEAIQKQEE
INFRLQDYID RIIVAILETN PSILEVK
//
